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Q8WYB5 (KAT6B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase KAT6B

EC=2.3.1.48
Alternative name(s):
Histone acetyltransferase MOZ2
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4
Short name=MYST-4
Monocytic leukemia zinc finger protein-related factor
Gene names
Name:KAT6B
Synonyms:KIAA0383, MORF, MOZ2, MYST4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2073 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Ref.1 Ref.7 Ref.8

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.1

Subunit structure

Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with RUNX1 and RUNX2. Ref.7 Ref.8 Ref.9

Subcellular location

Nucleus Probable.

Tissue specificity

Ubiquitously expressed, with high levels in heart, pancreas, testis and ovary. Ref.1

Domain

The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression. Ref.1

Post-translational modification

Autoacetylated. Ref.1 Ref.7

Autoacetylation at Lys-815 is required for proper function By similarity. Ref.1 Ref.7

Involvement in disease

A chromosomal aberration involving KAT6B may be a cause acute myeloid leukemias. Translocation t(10;16)(q22;p13) with CREBBP.

Ohdo syndrome, SBBYS variant (SBBYSS) [MIM:603736]: A syndrome characterized by distinctive facial appearance with severe blepharophimosis, an immobile mask-like face, a bulbous nasal tip, and a small mouth with a thin upper lip. The condition presents in infancy with severe hypotonia and feeding problems. Associated skeletal problems include joint laxity, abnormally long thumbs and great toes, and dislocated or hypoplastic patellae. Structural cardiac defects are present in around 50% of cases, and dental anomalies, including small and pointed teeth, are common. Optic atrophy and conductive or sensorineural deafness are repeatedly reported. Many affected individuals have abnormalities of thyroid structure or function. SBBYSS is usually associated with severe mental retardation, delayed motor milestones, and significantly impaired speech.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Genitopatellar syndrome (GTPTS) [MIM:606170]: A rare disorder consisting of microcephaly, severe psychomotor retardation, and characteristic coarse facial features, including broad nose and small or retracted chin, associated with congenital flexion contractures of the lower extremities, abnormal or missing patellae, and urogenital anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 C2HC-type zinc finger.

Contains 1 H15 (linker histone H1/H5 globular) domain.

Contains 2 PHD-type zinc fingers.

Sequence caution

The sequence AAF00100.1 differs from that shown. Reason: Frameshift at positions 550 and 562.

The sequence AAH14143.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH48199.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Repressor
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

histone H3 acetylation

Inferred from direct assay Ref.8. Source: UniProtKB

histone acetylation

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

nucleosome assembly

Non-traceable author statement Ref.1. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1Ref.7. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMOZ/MORF histone acetyltransferase complex

Inferred from direct assay Ref.8Ref.9. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleosome

Non-traceable author statement Ref.1. Source: UniProtKB

nucleus

Traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

acetyltransferase activity

Inferred from direct assay Ref.7. Source: UniProtKB

histone acetyltransferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

transcription factor binding

Inferred from direct assay Ref.7. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WYB5-1)

Also known as: Beta;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WYB5-2)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     482-664: Missing.
Isoform 3 (identifier: Q8WYB5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     373-664: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20732073Histone acetyltransferase KAT6B
PRO_0000051575

Regions

Domain103 – 17674H15
Zinc finger213 – 27260PHD-type 1
Zinc finger269 – 32052PHD-type 2
Zinc finger749 – 77123C2HC-type
Region361 – 717357Negatively regulates HAT activity
Region718 – 1008291Catalytic
Region752 – 1008257Interaction with BRPF1
Region856 – 8605Acetyl-CoA binding By similarity
Region865 – 8717Acetyl-CoA binding By similarity
Region1560 – 2073514Interaction with RUNX1 and RUNX2
Compositional bias492 – 53342Ser-rich
Compositional bias521 – 5244Poly-Ser
Compositional bias599 – 6057Poly-Ser
Compositional bias1070 – 110435Poly-Glu
Compositional bias1204 – 12074Poly-Glu
Compositional bias1351 – 137323Poly-Glu
Compositional bias1409 – 14179Poly-Glu
Compositional bias1594 – 1763170Ser-rich
Compositional bias1961 – 2061101Met-rich

Sites

Active site8151 By similarity
Active site8571Nucleophile By similarity
Binding site8951Acetyl-CoA By similarity
Site1222 – 12232Breakpoint for translocation to form KAT6B-CREBBP

Amino acid modifications

Modified residue8151N6-acetyllysine; by autocatalysis By similarity
Modified residue10381N6-acetyllysine Ref.10
Modified residue10421N6-acetyllysine Ref.10
Modified residue10441N6-acetyllysine Ref.10

Natural variations

Alternative sequence373 – 664292Missing in isoform 3.
VSP_014586
Alternative sequence482 – 664183Missing in isoform 2.
VSP_014587
Natural variant3601E → K. Ref.11
VAR_067315
Natural variant4831T → A in a breast cancer sample; somatic mutation. Ref.13
VAR_036361
Natural variant12171A → S.
Corresponds to variant rs57372986 [ dbSNP | Ensembl ].
VAR_061367
Natural variant14991V → I.
Corresponds to variant rs3740321 [ dbSNP | Ensembl ].
VAR_050217

Experimental info

Sequence conflict1231G → R in AAL56647. Ref.2
Sequence conflict2311P → A in AAL56647. Ref.2
Sequence conflict8431F → L in AAF00095. Ref.1
Sequence conflict8431F → L in AAF00099. Ref.1
Sequence conflict8431F → L in AAF00100. Ref.1
Sequence conflict8431F → L in BAA20837. Ref.3
Sequence conflict931 – 9333TGM → RHV in AAL56647. Ref.2
Sequence conflict9341Missing in AAL56647. Ref.2
Sequence conflict11521T → S in AAL56647. Ref.2
Sequence conflict16251S → T in AAL56647. Ref.2
Sequence conflict17311S → T in AAL56647. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Beta) [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: AEE267B9DA444B08

FASTA2,073231,378
        10         20         30         40         50         60 
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV 

        70         80         90        100        110        120 
LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK SAKGSRGSCN DLRNVDWNKL LRRAIEGLEE 

       130        140        150        160        170        180 
PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD 

       190        200        210        220        230        240 
GKGAPQYPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC 

       250        260        270        280        290        300 
GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC 

       310        320        330        340        350        360 
DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRLLSVTSDE 

       370        380        390        400        410        420 
GSMNAFTGRG SPGRGQKTKV CTTPSSGHAA SGKDSSSRLA VTDPTRPGAT TKITTTSTYI 

       430        440        450        460        470        480 
SASTLKVNKK TKGLIDGLTK FFTPSPDGRR SRGEIIDFSK HYRPRKKVSQ KQSCTSHVLA 

       490        500        510        520        530        540 
TGTTQKLKPP PSSLPPPTPI SGQSPSSQKS STATSSPSPQ SSSSQCSVPS LSSLTTNSQL 

       550        560        570        580        590        600 
KALFDGLSHI YTTQGQSRKK GHPSYAPPKR MRRKTELSST AKSKAHFFGK RDIRSRFISH 

       610        620        630        640        650        660 
SSSSSWGMAR GSIFKAIAHF KRTTFLKKHR MLGRLKYKVT PQMGTPSPGK GSLTDGRIKP 

       670        680        690        700        710        720 
DQDDDTEIKI NIKQESADVN VIGNKDVVTE EDLDVFKQAQ ELSWEKIECE SGVEDCGRYP 

       730        740        750        760        770        780 
SVIEFGKYEI QTWYSSPYPQ EYARLPKLYL CEFCLKYMKS KNILLRHSKK CGWFHPPANE 

       790        800        810        820        830        840 
IYRRKDLSVF EVDGNMSKIY CQNLCLLAKL FLDHKTLYYD VEPFLFYVLT KNDEKGCHLV 

       850        860        870        880        890        900 
GYFSKEKLCQ QKYNVSCIMI MPQHQRQGFG RFLIDFSYLL SRREGQAGSP EKPLSDLGRL 

       910        920        930        940        950        960 
SYLAYWKSVI LEYLYHHHER HISIKAISRA TGMCPHDIAT TLQHLHMIDK RDGRFVIIRR 

       970        980        990       1000       1010       1020 
EKLILSHMEK LKTCSRANEL DPDSLRWTPI LISNAAVSEE EREAEKEAER LMEQASCWEK 

      1030       1040       1050       1060       1070       1080 
EEQEILSTRA NSRQSPAKVQ SKNKYLHSPE SRPVTGERGQ LLELSKESSE EEEEEEDEEE 

      1090       1100       1110       1120       1130       1140 
EEEEEEEEED EEEEEEEEEE EEEENIQSSP PRLTKPQSVA IKRKRPFVLK KKRGRKRRRI 

      1150       1160       1170       1180       1190       1200 
NSSVTTETIS ETTEVLNEPF DNSDEERPMP QLEPTCEIEV EEDGRKPVLR KAFQHQPGKK 

      1210       1220       1230       1240       1250       1260 
RQTEEEEGKD NHCFKNADPC RNNMNDDSSN LKEGSKDNPE PLKCKQVWPK GTKRGLSKWR 

      1270       1280       1290       1300       1310       1320 
QNKERKTGFK LNLYTPPETP MEPDEQVTVE EQKETSEGKT SPSPIRIEEE VKETGEALLP 

      1330       1340       1350       1360       1370       1380 
QEENRREETC APVSPNTSPG EKPEDDLIKP EEEEEEEEEE EEEEEEEEGE EEEGGGNVEK 

      1390       1400       1410       1420       1430       1440 
DPDGAKSQEK EEPEISTEKE DSARLDDHEE EEEEDEEPSH NEDHDADDED DSHMESAEVE 

      1450       1460       1470       1480       1490       1500 
KEELPRESFK EVLENQETFL DLNVQPGHSN PEVLMDCGVD LTASCNSEPK ELAGDPEAVP 

      1510       1520       1530       1540       1550       1560 
ESDEEPPPGE QAQKQDQKNS KEVDTEFKEG NPATMEIDSE TVQAVQSLTQ ESSEQDDTFQ 

      1570       1580       1590       1600       1610       1620 
DCAETQEACR SLQNYTRADQ SPQIATTLDD CQQSDHSSPV SSVHSHPGQS VRSVNSPSVP 

      1630       1640       1650       1660       1670       1680 
ALENSYAQIS PDQSAISVPS LQNMETSPMM DVPSVSDHSQ QVVDSGFSDL GSIESTTENY 

      1690       1700       1710       1720       1730       1740 
ENPSSYDSTM GGSICGNGSS QNSCSYSNLT SSSLTQSSCA VTQQMSNISG SCSMLQQTSI 

      1750       1760       1770       1780       1790       1800 
SSPPTCSVKS PQGCVVERPP SSSQQLAQCS MAANFTPPMQ LAEIPETSNA NIGLYERMGQ 

      1810       1820       1830       1840       1850       1860 
SDFGAGHYPQ PSATFSLAKL QQLTNTLIDH SLPYSHSAAV TSYANSASLS TPLSNTGLVQ 

      1870       1880       1890       1900       1910       1920 
LSQSPHSVPG GPQAQATMTP PPNLTPPPMN LPPPLLQRNM AASNIGISHS QRLQTQIASK 

      1930       1940       1950       1960       1970       1980 
GHISMRTKSA SLSPAAATHQ SQIYGRSQTV AMQGPARTLT MQRGMNMSVN LMPAPAYNVN 

      1990       2000       2010       2020       2030       2040 
SVNMNMNTLN AMNGYSMSQP MMNSGYHSNH GYMNQTPQYP MQMQMGMMGT QPYAQQPMQT 

      2050       2060       2070 
PPHGNMMYTA PGHHGYMNTG MSKQSLNGSY MRR 

« Hide

Isoform 2 (Alpha) [UniParc].

Checksum: 9AD95D653693CFBA
Show »

FASTA1,890211,537
Isoform 3 [UniParc].

Checksum: 895F7DE8B12455E8
Show »

FASTA1,781199,858

References

« Hide 'large scale' references
[1]"Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein."
Champagne N., Bertos N.R., Pelletier N., Wang A.H., Vezmar M., Yang Y., Heng H.H., Yang X.-J.
J. Biol. Chem. 274:28528-28536(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, ACETYLATION, ENZYME ACTIVITY, DOMAIN, FUNCTION.
Tissue: Bone marrow.
[2]"Structure and function of the human MYST family: MOZ2, MYST1 and MYST2."
Borrow J., Housman D.E.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-322 AND 1187-2073.
Tissue: Brain and Lung.
[6]"Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13)."
Panagopoulos I., Fioretos T., Isaksson M., Samuelsson U., Billstroem R., Stroembeck B., Mitelman F., Johansson B.
Hum. Mol. Genet. 10:395-404(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1136-1287, CHROMOSOMAL TRANSLOCATION WITH CREBBP.
[7]"MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2."
Pelletier N., Champagne N., Stifani S., Yang X.-J.
Oncogene 21:2729-2740(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUNX1 AND RUNX2, ACETYLATION, FUNCTION.
[8]"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
[9]"Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes."
Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C., Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J., Yang X.-J.
Mol. Cell. Biol. 28:6828-6843(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1038; LYS-1042 AND LYS-1044, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Whole-exome-sequencing identifies mutations in histone acetyltransferase gene KAT6B in individuals with the Say-Barber-Biesecker variant of Ohdo syndrome."
Clayton-Smith J., O'Sullivan J., Daly S., Bhaskar S., Day R., Anderson B., Voss A.K., Thomas T., Biesecker L.G., Smith P., Fryer A., Chandler K.E., Kerr B., Tassabehji M., Lynch S.A., Krajewska-Walasek M., McKee S., Smith J. expand/collapse author list , Sweeney E., Mansour S., Mohammed S., Donnai D., Black G.
Am. J. Hum. Genet. 89:675-681(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SBBYSS, VARIANT LYS-360.
[12]"Mutations in KAT6B, encoding a histone acetyltransferase, cause Genitopatellar syndrome."
Campeau P.M., Kim J.C., Lu J.T., Schwartzentruber J.A., Abdul-Rahman O.A., Schlaubitz S., Murdock D.M., Jiang M.M., Lammer E.J., Enns G.M., Rhead W.J., Rowland J., Robertson S.P., Cormier-Daire V., Bainbridge M.N., Yang X.J., Gingras M.C., Gibbs R.A. expand/collapse author list , Rosenblatt D.S., Majewski J., Lee B.H.
Am. J. Hum. Genet. 90:282-289(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GTPTS.
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-483.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF113514 mRNA. Translation: AAF00095.1.
AF119230 mRNA. Translation: AAF00099.1.
AF119231 mRNA. Translation: AAF00100.1. Frameshift.
AF217500 mRNA. Translation: AAL56647.1.
AB002381 mRNA. Translation: BAA20837.2.
BC014143 mRNA. Translation: AAH14143.1. Sequence problems.
BC021128 mRNA. Translation: AAH21128.1.
BC048199 mRNA. Translation: AAH48199.1. Sequence problems.
CCDSCCDS58084.1. [Q8WYB5-3]
CCDS58085.1. [Q8WYB5-2]
CCDS7345.1. [Q8WYB5-1]
RefSeqNP_001243397.1. NM_001256468.1. [Q8WYB5-2]
NP_001243398.1. NM_001256469.1. [Q8WYB5-3]
NP_036462.2. NM_012330.3. [Q8WYB5-1]
XP_005269721.1. XM_005269664.1. [Q8WYB5-1]
UniGeneHs.35758.
Hs.599543.
Hs.740873.

3D structure databases

ProteinModelPortalQ8WYB5.
SMRQ8WYB5. Positions 211-320, 718-990.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117069. 10 interactions.
IntActQ8WYB5. 3 interactions.
MINTMINT-2871056.
STRING9606.ENSP00000287239.

PTM databases

PhosphoSiteQ8WYB5.

Polymorphism databases

DMDM143811424.

Proteomic databases

MaxQBQ8WYB5.
PaxDbQ8WYB5.
PRIDEQ8WYB5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287239; ENSP00000287239; ENSG00000156650. [Q8WYB5-1]
ENST00000372711; ENSP00000361796; ENSG00000156650. [Q8WYB5-2]
ENST00000372714; ENSP00000361799; ENSG00000156650. [Q8WYB5-3]
ENST00000372724; ENSP00000361809; ENSG00000156650. [Q8WYB5-3]
ENST00000372725; ENSP00000361810; ENSG00000156650. [Q8WYB5-3]
GeneID23522.
KEGGhsa:23522.
UCSCuc001jwm.2. human. [Q8WYB5-3]
uc001jwn.2. human. [Q8WYB5-1]
uc031pvy.1. human. [Q8WYB5-2]

Organism-specific databases

CTD23522.
GeneCardsGC10P076586.
GeneReviewsKAT6B.
HGNCHGNC:17582. KAT6B.
HPAHPA006104.
MIM603736. phenotype.
605880. gene.
606170. phenotype.
neXtProtNX_Q8WYB5.
Orphanet3047. Blepharophimosis-intellectual disability syndrome, SBBYS type.
85201. Genitopatellar syndrome.
648. Noonan syndrome.
PharmGKBPA134880712.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5027.
HOVERGENHBG052563.
InParanoidQ8WYB5.
KOK11306.
OMALRWTPIL.
OrthoDBEOG7WHH8N.
PhylomeDBQ8WYB5.
TreeFamTF106483.

Enzyme and pathway databases

BRENDA2.3.1.48. 2681.
ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ8WYB5.
BgeeQ8WYB5.
CleanExHS_MYST4.
GenevestigatorQ8WYB5.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.30.40.10. 1 hit.
3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00538. Linker_histone. 1 hit.
PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS51504. H15. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKAT6B. human.
GeneWikiMYST4.
GenomeRNAi23522.
NextBio45977.
PROQ8WYB5.
SOURCESearch...

Entry information

Entry nameKAT6B_HUMAN
AccessionPrimary (citable) accession number: Q8WYB5
Secondary accession number(s): O15087 expand/collapse secondary AC list , Q86Y05, Q8WU81, Q9UKW2, Q9UKW3, Q9UKX0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM